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Conserved domains on  [gi|2464176415|ref|NP_001405673|]
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valacyclovir hydrolase isoform 4 [Mus musculus]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 25-189 1.11e-26

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 100.85  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  25 ALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIwganayVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYlaktc 104
Cdd:COG0596    85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALARTDL----- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 105 edwvdgisqfkqlpegnicRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGSRLHLMPEGKHNLHLRFADEFNRLV 184
Cdd:COG0596   154 -------------------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAAL 214


                  ....*
gi 2464176415 185 EDFLQ 189
Cdd:COG0596   215 RDFLA 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 25-189 1.11e-26

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 100.85  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  25 ALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIwganayVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYlaktc 104
Cdd:COG0596    85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALARTDL----- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 105 edwvdgisqfkqlpegnicRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGSRLHLMPEGKHNLHLRFADEFNRLV 184
Cdd:COG0596   154 -------------------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAAL 214


                  ....*
gi 2464176415 185 EDFLQ 189
Cdd:COG0596   215 RDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 25-174 7.23e-13

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 64.83  E-value: 7.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  25 ALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIWGANAYVTEEDSRIYQGIRDVSKWSEKAR-------------KPL 91
Cdd:pfam00561  65 ALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVadfapnplgrlvaKLL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  92 EALYGYDYLAKTCEDW---------------VDGISQFKQLPEGNICRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQH 156
Cdd:pfam00561 145 ALLLLRLRLLKALPLLnkrfpsgdyalakslVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQL 224

                         170
                  ....*....|....*...
gi 2464176415 157 VKGSRLHLMPEGKHNLHL 174
Cdd:pfam00561 225 FPNARLVVIPDAGHFAFL 242
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 25-189 1.11e-26

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 100.85  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  25 ALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIwganayVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYlaktc 104
Cdd:COG0596    85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALARTDL----- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 105 edwvdgisqfkqlpegnicRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGSRLHLMPEGKHNLHLRFADEFNRLV 184
Cdd:COG0596   154 -------------------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAAL 214


                  ....*
gi 2464176415 185 EDFLQ 189
Cdd:COG0596   215 RDFLA 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
27-189 4.16e-19

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 81.53  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  27 QFKQVSLLGWSDGGITALIAAAKYPSyIRKMVIWGANAYVTEEDSRI----YQGIRDVSKWSEKARKPLEALYGYDYLak 102
Cdd:COG1647    82 GYDKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLlpllKYLARSLRGIGSDIEDPEVAEYAYDRT-- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 103 tcedWVDGISQFKQLpeGNICRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGS--RLHLMPEGKHNLHL-RFADE 179
Cdd:COG1647   159 ----PLRALAELQRL--IREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELVWLEDSGHVITLdKDREE 232

                         170
                  ....*....|
gi 2464176415 180 FNRLVEDFLQ 189
Cdd:COG1647   233 VAEEILDFLE 242
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 25-174 7.23e-13

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 64.83  E-value: 7.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  25 ALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIWGANAYVTEEDSRIYQGIRDVSKWSEKAR-------------KPL 91
Cdd:pfam00561  65 ALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVadfapnplgrlvaKLL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  92 EALYGYDYLAKTCEDW---------------VDGISQFKQLPEGNICRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQH 156
Cdd:pfam00561 145 ALLLLRLRLLKALPLLnkrfpsgdyalakslVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQL 224

                         170
                  ....*....|....*...
gi 2464176415 157 VKGSRLHLMPEGKHNLHL 174
Cdd:pfam00561 225 FPNARLVVIPDAGHFAFL 242
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
29-188 1.24e-11

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 61.19  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  29 KQVSLLGWSDGGITALIAAAKYPSYIRKMVIWGANAYVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYLAKtcedwv 108
Cdd:COG1506    93 DRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAARSPLAYADK------ 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 109 dgisqfkqlpegnicrhllplVQCPTLIVHGEKDPLVPRFHA----DFLLQHVKGSRLHLMPEGKHNLHLRFADEFNRLV 184
Cdd:COG1506   167 ---------------------LKTPLLLIHGEADDRVPPEQAerlyEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERI 225


                  ....
gi 2464176415 185 EDFL 188
Cdd:COG1506   226 LDFL 229
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-189 4.41e-11

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 59.63  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  29 KQVSLLGWSDGGITALIAAAKYPSYIRKMVIWGAnAYVTEEDSRIYQGIrdvskwsekarkpLEALYGYDYLAKtcedwv 108
Cdd:COG2267    99 LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP-AYRADPLLGPSARW-------------LRALRLAEALAR------ 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 109 dgisqfkqlpegnicrhllplVQCPTLIVHGEKDPLVPRFHADFLLQHV-KGSRLHLMPEGKHNLHL-RFADEFNRLVED 186
Cdd:COG2267   159 ---------------------IDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNePAREEVLAAILA 217


                  ...
gi 2464176415 187 FLQ 189
Cdd:COG2267   218 WLE 220
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 33-189 4.70e-07

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 48.37  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  33 LLGWSDGGITALIAAAKYPsyirkmviwGANAYVTeeDS---RIYQGIRDVSKWSEKARKPlealyGYDYLAK-TCEDWV 108
Cdd:COG1073   113 LLGISLGGGYALNAAATDP---------RVKAVIL--DSpftSLEDLAAQRAKEARGAYLP-----GVPYLPNvRLASLL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 109 -DGISQFKQLPEgnicrhllplVQCPTLIVHGEKDPLVPRFHADFLLQHVKGS-RLHLMPEGKHN-LHLRFADEFNRLVE 185
Cdd:COG1073   177 nDEFDPLAKIEK----------ISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPkELLIVPGAGHVdLYDRPEEEYFDKLA 246


                  ....
gi 2464176415 186 DFLQ 189
Cdd:COG1073   247 EFFK 250
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 27-183 1.57e-04

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 40.92  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  27 QFKQVSLLGWSDGGITALIAAAkypSYIRKMVIWGANAYVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYLAKTCED 106
Cdd:pfam12697  57 AARPVVLVGHSLGGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPAD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415 107 --WVDGISQFKQLPEGN--ICRHLLPLVQCPTLIVHGEkDPLVPRFHADfLLQHVKGSRLHLMPEGKHNLHLRfADEFNR 182
Cdd:pfam12697 134 aeWAAALARLAALLAALalLPLAAWRDLPVPVLVLAEE-DRLVPELAQR-LLAALAGARLVVLPGAGHLPLDD-PEEVAE 210


                  .
gi 2464176415 183 L 183
Cdd:pfam12697 211 A 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 33-173 3.74e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.89  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  33 LLGWSDGGITALIAAAKYPSYIRKMVIWGANAYVTEED------------SRIYQGIR--------DVSKWSEKARKple 92
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLappilkllakllGKLFPRLRvpnnllpdSLSRDPEVVAA--- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2464176415  93 alYGYDylaktcEDWVDGIS-----QFKQLpeGNICRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGS--RLHLM 165
Cdd:pfam12146 157 --YAAD------PLVHGGISartlyELLDA--GERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLY 226


                  ....*...
gi 2464176415 166 PEGKHNLH 173
Cdd:pfam12146 227 PGLYHELL 234
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
127-189 9.64e-04

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 38.60  E-value: 9.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2464176415 127 LPLVQCPTLIVHGEKDPLVPRFHA-DFLLQHVKGSRLHLMPEGKHNLHlRFADEFNRLVEDFLQ 189
Cdd:COG2945   138 LAPCPAPTLVIHGEQDEVVPPAEVlDWARPLSPPLPVVVVPGADHFFH-GKLDELKELVARYLP 200
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 133-146 1.41e-03

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 37.93  E-value: 1.41e-03
                          10
                  ....*....|....
gi 2464176415 133 PTLIVHGEKDPLVP 146
Cdd:pfam20434 191 PFLIIHGDKDPLVP 204
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 127-175 4.06e-03

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 36.41  E-value: 4.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2464176415 127 LPLVQCPTLIVHGEKDPLVPRfhaDFL--LQHVKGSRLHLMPEGKHNLHLR 175
Cdd:pfam20408 123 LPDLTCPTLILQGERDPFGNR---EEVaaYPLPDNVSLHWLEDGDHDFKPR 170
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
126-188 4.55e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 36.48  E-value: 4.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2464176415 126 LLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGS----RLHLMPEGKHNLHLRFADEFN--------RLVEDFL 188
Cdd:COG0412   151 LAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAgvdvELHVYPGAGHGFTNPGRPRYDpaaaedawQRTLAFL 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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